DOI: 10.1073/pnas.082100499. Catalysis of cis/trans isomerization in native HIV-1 capsid by human cyclophilin A

Catalysis of cis/trans isomerization in native HIV-1 capsid by human cyclophilin A

10.1073/pnas.082100499

Crossref journal-article

Proceedings of the National Academy of Sciences

Proceedings of the National Academy of Sciences (341)

Abstract

Packaging of cyclophilin A (CypA) into HIV-1 virions is essential for efficient replication; however, the reason for this is unknown. Incorporation is mediated through binding to the Gly-89–Pro-90 peptide bond of the N-terminal domain of HIV-1 capsid (CA N ). Despite the fact that CypA is a peptidyl-prolyl cis/trans isomerase, catalytic activity on CA N has not been observed previously. We show here, using NMR exchange spectroscopy, that CypA does not only bind to CA N but also catalyzes efficiently the cis/trans isomerization of the Gly-89–Pro-90 peptide bond. In addition, conformational changes in CA N distal to the CypA binding loop are observed on CypA binding and catalysis. The results provide experimental evidence for efficient CypA catalysis on a natively folded and biologically relevant protein substrate.

Bibliography

Bosco, D. A., Eisenmesser, E. Z., Pochapsky, S., Sundquist, W. I., & Kern, D. (2002). Catalysis of cis/trans isomerization in native HIV-1 capsid by human cyclophilin A. Proceedings of the National Academy of Sciences, 99(8), 5247â5252.

Authors 5

Daryl A. Bosco (first)
Elan Z. Eisenmesser (additional)
Susan Pochapsky (additional)
Wesley I. Sundquist (additional)
Dorothee Kern (additional)

References 63 Referenced 185

Dates

Type	When
Created	23 years ago (July 26, 2002, 10:45 a.m.)
Deposited	3 years, 4 months ago (April 12, 2022, 6:24 p.m.)
Indexed	1 month ago (July 24, 2025, 7:44 a.m.)
Issued	23 years, 4 months ago (April 2, 2002)
Published	23 years, 4 months ago (April 2, 2002)
Published Online	23 years, 4 months ago (April 2, 2002)
Published Print	23 years, 4 months ago (April 16, 2002)

Funders 0

None

BibTeX

@article{Bosco_2002, title={Catalysis of cis/trans isomerization in native HIV-1 capsid by human cyclophilin A}, volume={99}, ISSN={1091-6490}, url={http://dx.doi.org/10.1073/pnas.082100499}, DOI={10.1073/pnas.082100499}, number={8}, journal={Proceedings of the National Academy of Sciences}, publisher={Proceedings of the National Academy of Sciences}, author={Bosco, Daryl A. and Eisenmesser, Elan Z. and Pochapsky, Susan and Sundquist, Wesley I. and Kern, Dorothee}, year={2002}, month=apr, pages={5247–5252} }

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  "abstract": "<jats:p>\n            Packaging of cyclophilin A (CypA) into HIV-1 virions is essential for efficient replication; however, the reason for this is unknown. Incorporation is mediated through binding to the Gly-89\u2013Pro-90 peptide bond of the N-terminal domain of HIV-1 capsid (CA\n            <jats:sup>N</jats:sup>\n            ). Despite the fact that CypA is a peptidyl-prolyl cis/trans isomerase, catalytic activity on CA\n            <jats:sup>N</jats:sup>\n            has not been observed previously. We show here, using NMR exchange spectroscopy, that CypA does not only bind to CA\n            <jats:sup>N</jats:sup>\n            but also catalyzes efficiently the cis/trans isomerization of the Gly-89\u2013Pro-90 peptide bond. In addition, conformational changes in CA\n            <jats:sup>N</jats:sup>\n            distal to the CypA binding loop are observed on CypA binding and catalysis. The results provide experimental evidence for efficient CypA catalysis on a natively folded and biologically relevant protein substrate.\n          </jats:p>",
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